Lignin peroxidase of Phanerochaete chrysosporium. Evidence for an acidic ionization controlling activity.

@article{Cai1991LigninPO,
  title={Lignin peroxidase of Phanerochaete chrysosporium. Evidence for an acidic ionization controlling activity.},
  author={Da Yong Cai and Ming Tien},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 22},
  pages={
          14464-9
        }
}
The active site amino acid residues of lignin peroxidase are homologous to those of other peroxidases; however, in contrast to other peroxidases, no pH dependence is observed for the reaction of ferric lignin peroxidase with H2O2 to form compound I (Andrawis, A., Johnson, K.A., and Tien, M. (1988) J. Biol. Chem. 263, 1195-1198). Chloride binding is used in the present study to investigate this reaction further. Chloride binds to lignin peroxidase at the same site as cyanide and hydrogen… CONTINUE READING

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